PK22_PSEAE
ID PK22_PSEAE Reviewed; 496 AA.
AC Q9HYF1;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Polyphosphate:AMP phosphotransferase {ECO:0000305};
DE Short=PAP {ECO:0000250|UniProtKB:Q83XD3};
DE EC=2.7.4.33 {ECO:0000269|PubMed:19001261};
DE AltName: Full=Polyphosphate kinase PPK2 3 {ECO:0000305};
GN OrderedLocusNames=PA3455 {ECO:0000312|EMBL:AAG06843.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007744|PDB:3CZP}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, AND MUTAGENESIS
RP OF GLU-304; ASP-307; LYS-311; ARG-316; ASP-320; ASP-323; ARG-325; ASP-362;
RP ARG-363; TRP-408; GLN-416; ARG-419; ARG-423; ASP-437; TYR-447; LYS-473 AND
RP ARG-477.
RX PubMed=19001261; DOI=10.1073/pnas.0807563105;
RA Nocek B., Kochinyan S., Proudfoot M., Brown G., Evdokimova E., Osipiuk J.,
RA Edwards A.M., Savchenko A., Joachimiak A., Yakunin A.F.;
RT "Polyphosphate-dependent synthesis of ATP and ADP by the family-2
RT polyphosphate kinases in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17730-17735(2008).
CC -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC AMP to ADP. Can also convert GMP to GDP, with lower efficiency. Cannot
CC dephosphorylate ADP in the presence of polyP.
CC {ECO:0000269|PubMed:19001261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + ADP = [phosphate](n+1) + AMP;
CC Xref=Rhea:RHEA:57820, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.4.33; Evidence={ECO:0000269|PubMed:19001261};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19001261};
CC Note=Has low activity with Co(2+) or Ni(2+).
CC {ECO:0000269|PubMed:19001261};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-9.5. {ECO:0000269|PubMed:19001261};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19001261}.
CC -!- INTERACTION:
CC Q9HYF1; Q9HYF1: PA3455; NbExp=2; IntAct=EBI-15739712, EBI-15739712;
CC -!- DOMAIN: Contains 2 fused PPK2 domains. The N-terminal domain seems to
CC be catalytically inactive and might be responsible for the protein
CC dimerization. {ECO:0000269|PubMed:19001261}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC II subfamily. {ECO:0000305}.
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DR EMBL; AE004091; AAG06843.1; -; Genomic_DNA.
DR PIR; F83213; F83213.
DR RefSeq; NP_252145.1; NC_002516.2.
DR RefSeq; WP_003091935.1; NZ_QZGE01000037.1.
DR PDB; 3CZP; X-ray; 2.00 A; A/B=1-496.
DR PDBsum; 3CZP; -.
DR AlphaFoldDB; Q9HYF1; -.
DR SMR; Q9HYF1; -.
DR DIP; DIP-48618N; -.
DR STRING; 287.DR97_4466; -.
DR PaxDb; Q9HYF1; -.
DR PRIDE; Q9HYF1; -.
DR EnsemblBacteria; AAG06843; AAG06843; PA3455.
DR GeneID; 878853; -.
DR KEGG; pae:PA3455; -.
DR PATRIC; fig|208964.12.peg.3617; -.
DR PseudoCAP; PA3455; -.
DR HOGENOM; CLU_033786_1_2_6; -.
DR InParanoid; Q9HYF1; -.
DR OMA; SPLDWQQ; -.
DR PhylomeDB; Q9HYF1; -.
DR BioCyc; PAER208964:G1FZ6-3523-MON; -.
DR BRENDA; 2.7.4.33; 5087.
DR EvolutionaryTrace; Q9HYF1; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0043751; F:polyphosphate:AMP phosphotransferase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006797; P:polyphosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022489; PolyP_AMP_Tfrase.
DR InterPro; IPR022488; PPK2-related.
DR Pfam; PF03976; PPK2; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03708; poly_P_AMP_trns; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Kinase; Magnesium; Reference proteome; Repeat; Transferase.
FT CHAIN 1..496
FT /note="Polyphosphate:AMP phosphotransferase"
FT /id="PRO_0000442597"
FT REGION 11..234
FT /note="PPK2 1"
FT /evidence="ECO:0000305"
FT REGION 269..495
FT /note="PPK2 2"
FT /evidence="ECO:0000305"
FT MUTAGEN 304
FT /note="E->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 307
FT /note="D->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 311
FT /note="K->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 316
FT /note="R->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 320
FT /note="D->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 323
FT /note="D->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 325
FT /note="R->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 362
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 363
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 408
FT /note="W->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 416
FT /note="Q->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 419
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 423
FT /note="R->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 437
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 447
FT /note="Y->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 473
FT /note="K->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 477
FT /note="R->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 13..37
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 123..142
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 184..201
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 216..236
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 271..290
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 380..399
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 402..410
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:3CZP"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 444..458
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:3CZP"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:3CZP"
FT HELIX 473..494
FT /evidence="ECO:0007829|PDB:3CZP"
SQ SEQUENCE 496 AA; 58331 MW; 6BA1C283EA5C53E5 CRC64;
MFESAEVGHS IDKDTYEKAV IELREALLEA QFELKQQARF PVIILINGIE GAGKGETVKL
LNEWMDPRLI EVQSFLRPSD EELERPPQWR FWRRLPPKGR TGIFFGNWYS QMLYARVEGH
IKEAKLDQAI DAAERFERML CDEGALLFKF WFHLSKKQLK ERLKALEKDP QHSWKLSPLD
WKQSEVYDRF VHYGERVLRR TSRDYAPWYV VEGADERYRA LTVGRILLEG LQAALATKER
AKRQPHAAPL VSSLDNRGLL DSLDLGQYLD KDAYKEQLAA EQARLAGLIR DKRFRQHSLV
AVFEGNDAAG KGGAIRRVTD ALDPRQYHIV PIAAPTEEER AQPYLWRFWR HIPARRQFTI
FDRSWYGRVL VERIEGFCAP ADWLRAYGEI NDFEEQLSEY GIIVVKFWLA IDKQTQMERF
KEREKTPYKR YKITEEDWRN RDKWDQYVDA VGDMVDRTST EIAPWTLVEA NDKRFARVKV
LRTINDAIEA AYKKDK
